The function of alpha-crystallin in vision

Semin Cell Dev Biol. 2000 Feb;11(1):53-60. doi: 10.1006/scdb.1999.0351.

Abstract

The alpha-crystallins account for approximately one-third of the total soluble protein in the lens, contributing to its refractive power. In addition, alpha-crystallin also has a chaperone-like function and thus can bind unfolding lens proteins. Alpha B-crystallin is also found outside the lens, having an extensive tissue distribution. It is over-expressed in response to stresses of all kinds, where it is thought to serve a general protective function. Recently, it has been shown in humans that naturally occurring point mutations in the alpha-crystallins result in a deficit in chaperone-like function, and cause cataracts as well as a desmin-related myopathy. This review summarizes much of the past and current knowledge concerning the structure and functions of alpha-crystallin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Crystallins / genetics
  • Crystallins / pharmacology
  • Crystallins / physiology*
  • Humans
  • Lens, Crystalline / chemistry
  • Molecular Chaperones
  • Mutation
  • Vision, Ocular / drug effects
  • Vision, Ocular / physiology*

Substances

  • Crystallins
  • Molecular Chaperones